New caerin 1 antibiotic peptides from the skin secretion of the Australian tree frog Litoria chloris. Part 2. Sequence determination using electrospray mass spectrometry.
Electrospray mass spectrometry and automated Edman sequencing provides the structures of two new caerin 1 antimicrobial peptides from the skin glands of the Australian tree frog Litoria chloris. These are: caerin 1.8 Gly Leu Phe Lys Val Leu Gly Ser Val Ala Lys His Leu Leu Pro His Val Val Pro Val Ile Ala Glu Lys Leu (NH2), and caerin 1.9, Gly Leu Phe Gly Val Leu Gly Ser Ile Ala Lys His Val Leu Pro His Val Val Pro Val Ile Ala Glu Lys Leu (NH2).
Wabnitz
P A
PA
Department of Chemistry, University of Adelaide, Australia.
Steinborner
S T
ST
Currie
G J
GJ
Bowie
J H
JH
Tyler
M J
MJ
D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000890:Anti-Infective Agents / Q000032:analysis*; D023181:Antimicrobial Cationic Peptides; D001001:Anura / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis*; D012867:Skin / Q000737:chemistry*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C110755:caerin 1.8 protein, Litoria; C110757:caerin 1.9 protein, Litoria